Gadolinium(III) as a paramagnetic probe for proton relaxation studies of biological macromolecules. Binding to bovine serum albumin

Biochemistry ◽  
1971 ◽  
Vol 10 (15) ◽  
pp. 2834-2838 ◽  
Author(s):  
Jacques Reuben
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Proton Relaxation ◽  
Biological Macromolecules ◽  
Paramagnetic Probe ◽  
Relaxation Studies

Bovine Serum Albumin-Directed Fabrication of Nanohydroxyapatite with Improved Stability and Biocompatibility

2021 ◽  
pp. 2150028
Author(s):  
Ting Li ◽  
Jialu Yu ◽  
Hao Sui ◽  
Tao Zhang ◽  
Ronghui Zhou
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Bone Repair ◽  
Practical Importance ◽  
Biomimetic Synthesis ◽  
Biological Macromolecules ◽  
Reaction Conditions ◽  
Physical Conditions ◽  
Improved Stability

Nanohydroxyapatite (nHAp) has gained considerable concerns due to its vast potential in biomedical applications such as drug delivery, tissue engineering and bone repair. However, the preparation of HAp nanostructures in a controllable manner under environment-friendly reaction conditions remains a challenge. In recent years, the use of biological macromolecules or proteins as templates in the production of nanomaterials has gained more attention due to the relatively mild physical conditions needed for biomimetic synthesis. In this study, a novel nHAp was fabricated by employing bovine serum albumin (BSA) as template under mild condition. After that, the as-obtained nanostructured materials which have well-defined structures and morphologies were characterized by various methods. Furthermore, the rod-like shaped hydroxyapatite demonstrated improved stability properties, as well as cell viability and biocompatibility, compared to BSA free synthesized c-HAp. We expect that this pleasantly novel research will render new insights into the fabrication strategies of nanomaterials and be of practical importance for the expanding biological application.

Vitro toxicity assessments of nano-ZnS on bovine serum albumin by multispectroscopic methods

2016 ◽  
Vol 94 (10) ◽  
pp. 877-881
Author(s):  
Caishuang Liang ◽  
Xiaoqing Liu ◽  
Chunyan Chen ◽  
Xiaoming Chen ◽  
Changqun Cai
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Resonance Light Scattering ◽  
Toxic Effects ◽  
Biological Macromolecules ◽  
Mechanisms Of Toxicity ◽  
Hydrophobic Amino Acids ◽  
New Perspective ◽  
Insight Into

Measuring protein damaged by nanomaterials may give insight into the mechanisms of toxicity of nanomaterials. The toxic effects of nano-ZnS, nano-Al2O3, nano-ZnCO3, and nano-SiO2 on bovine serum albumin (BSA) were thoroughly studied by multispectroscopic methods, including resonance light scattering, UV-vis absorption spectroscopy, fluorescence spectroscopy, circular dichroism, etc., and the most obvious changes were observed when nano-ZnS interacted with BSA among the four nanoparticles. The experimental results showed that nano-ZnS can bind with BSA to form a complex when the conjugating ratio is 1:1. nano-ZnS can alter the structure of BSA, leading to a loosening of the protein skeleton, and therefore, the internal hydrophobic amino acids are exposed in the loose structure, which indicated that nano-ZnS has an obvious toxic effect on BSA. This work provides a new perspective and method for determining the toxic effects of nanomaterials on biological macromolecules.

Comparative intermolecular cross-relaxation studies of human hemoglobin in red blood cells and bovine serum albumin in solution

2011 ◽  
Vol 24 (5) ◽  
pp. 483-491 ◽  
Author(s):  
Seiichi Era ◽  
Masaru Sogami ◽  
Nobuhiro Uyesaka ◽  
Kazuo Kato ◽  
Masataka Murakami ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Bovine Serum ◽  
Cross Relaxation ◽  
Human Hemoglobin ◽  
Relaxation Studies

Chemical relaxation studies on bovine serum albumin

FEBS Letters ◽  
1974 ◽  
Vol 41 (1) ◽  
pp. 43-45 ◽  
Author(s):  
Herbert B. Silber ◽  
Julie A. Rosen
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Chemical Relaxation ◽  
Relaxation Studies

Improvement of an artificial test substrate technique for evaluation of em immunocytochemical labeling

1987 ◽  
Vol 45 ◽  
pp. 762-763
Author(s):  
G. D. Gagne ◽  
M. F. Miller
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Artificial Substrate ◽  
Chemical Fixation ◽  
As If

We recently described an artificial substrate system which could be used to optimize labeling parameters in EM immunocytochemistry (ICC). The system utilizes blocks of glutaraldehyde polymerized bovine serum albumin (BSA) into which an antigen is incorporated by a soaking procedure. The resulting antigen impregnated blocks can then be fixed and embedded as if they are pieces of tissue and the effects of fixation, embedding and other parameters on the ability of incorporated antigen to be immunocyto-chemically labeled can then be assessed. In developing this system further, we discovered that the BSA substrate can also be dried and then sectioned for immunolabeling with or without prior chemical fixation and without exposing the antigen to embedding reagents. The effects of fixation and embedding protocols can thus be evaluated separately.

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